SEMINAR

The interaction between transcription factors Sp1 and TAF4 via the intrinsically disordered regions

Abstract
Many transcription factors contain Glutamine-rich domains (Q-domains) which are considered to be important for molecular recognition. The transcription factors Sp1 and TAF4 are proposed to interact via their Q-domains. However, structural characterization of these Q-domains has not been performed, and the molecular mechanism of the interaction is still unclear. We measured NMR, CD, SPR, SAXS and SANS of Q-domain fragments of Sp1 and TAF4. The results revealed that all these Q-domains were kind of intrinsically disordered proteins (IDPs). The analisys indicated that Sp1 formed homo oligomers weakly by themselves and hetero oligomers with TAF4 site-specifically. Interestingly, no significant conformational change was observed upon oligomer formations. This may be a novel binding mode of IDPs.

BIOGRAPHY

2004-present: Associate Professor, Graduate School of Pharmaceutical Sciences, Kyoto University
2004: Visiting Fellow, Research School of Chemistry, Australian National University
1998-2004: Research Assistant, Institute for Protein Research, Osaka University
1998: PhD, Graduate School of Science, Osaka University

Research Fields and Interests:
Recent advances in protein science revealed that a protein structure is not necessarily a unique “static” conformation, but is changing dynamically depending on the environment. Such a variety of conformational change is closely related to the protein functions, exemplified by a coupled folding and binding of intrinsically disordered proteins, and fibril formation of amyloidogenic proteins. We focus on the “dynamic” nature of proteins upon interaction with biomolecules by using a various biophysical techniques.

Selected Publications:
S. Ishino, Y. Kawata, H. Taguchi, N. Kajimura, K. Matsuzaki & M. Hoshino (2015) Effects of C-terminal Truncation of Chaperonin GroEL on the Yield of In-cage Folding of the Green Fluorescent Protein. J. Biol. Chem. 290, 15042-15051.

S. Ishino, Y. Kawata, T. Ikegami, K. Matsuzaki & M. Hoshino (2014) Evaluation of the stability of an SR398/GroES chaperonin complex. J. Biochemistry 155, 295-300.

T. Yamaguchi, K. Matsuzaki & M. Hoshino (2013) Interaction between soluble AB(1–40) monomer and AB(1–42) fibrils probed by paramagnetic relaxation enhancement. FEBS Lett. 587, 620-624.

N. Hiramatsu, E. Hibino, K. Matsuzaki, J. Kuwahara & M. Hoshino (2012) Interaction between isolated transcriptional activation domains of Sp1 revealed by heteronuclear magnetic resonance. Protein Sci. 21, 1481-1488.

T. Yamaguchi, K. Matsuzaki & M. Hoshino (2011) Transient formation of intermediate conformational states of amyloid-B peptide revealed by heteronuclear magnetic resonance spectroscopy. FEBS Lett. 585, 1097-1102.